Measured by its binding ability in a functional ELISA. Immobilized rhGlypican 1 at 3 µg/mL (100 µL/well) will bind rhFGF-basic with an apparent KD < 1 nM.
Source
Mouse myeloma cell line, NS0-derived human Glypican 1 protein Asp24-Ser530, with a C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
56.8 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60 kDa, reducing conditions
Publications
Read Publications using 4519-GP in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Glypican 1 Protein, CF
FLJ38078
Glypican 1
glypican proteoglycan 1
glypican
glypican-1
GPC1
Background
The Glypicans (glypiated proteoglycans) are a small multigene family of GPI-linked proteoglycans that play a key role in growth factor signaling (1, 2, 3, 4). There are six known mammalian Glypicans. They all share a common-sized protein core of 60 - 70 kDa, an N-terminus which likely forms a compact globular domain, 14 conserved cysteines that form multiple intrachain disulfide bonds, and a number of C-terminal N- and O-linked carbohydrate attachment sites. Based on exon organization and the location of O-linked glycosylation sites, at least two subfamilies of Glypicans are known, with one subfamily containing Glypicans 1, 2, 4 and 6, and another subfamily containing Glypicans 3 and 5 (3, 5). Human Glypican 1 (GPC-1) is synthesized as a 558 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 aa mature segment, and a 28 aa C-terminal prosegment (6, 7). There are two potential N-linked and four potential O-linked sites for glycosylation or glycanation. There are potentially two heparan sulfate (HS) modifications on GPC-1 that could contribute to a native molecular weight of approximately 200 kDa (7, 8, 9). Mature human GPC-1 shares 91% aa identity with mature mouse GPC-1. There are two potential splice variants of human GPC-1. Both show an alternate start site at Met73, while one has an additional 65 aa substitution for the C-terminal 264 amino acids (10, 11). Cells known to express GPC-1 include neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumor-associated vascular endothelial cells (8, 9, 12 - 15). The function of GPC-1 is complex and varied. As a proteoglycan, it appears to make use of its HS adduct to impact select growth factor activity (16). This is accomplished by having juxtramembrane HS attachment sites, and a flexible, GPI-linkage (17). Data suggests GPC-1 and sulfation enzymes may collaborate to regulate FGF signaling. HS modules that are rich in 2-O- and 6-O- sulfate upregulate FGF-2 activation of FGFR1c (18). Similarly, FGF-1 requires both 2-O- and 6-O-sulfation to bind to FGFR2c and 3c. By contract, FGF-1 requires no sulfation to bind to FGFR2b, and FGF-8b needs only 6-O-sulfation to activate FGFR3c. Thus, many FGF receptor isoform specific effects may be attributed to an interaction between Glypican family members and the cell sulfation system (19).
Song, H.H. and J. Filmus (2002) Biochim. Biophys. Acta 1573:241.
Fransson, L-A. et al. (2004) Cell. Mol. Life Sci. 61:1016.
De Cat, B. and G. David (2001) Semin. Cell Dev. Biol. 12:117.
Lamoureux, F. et al. (2007) BioEssays 29:758.
Veugelers, M. et al. (1999) J. Biol. Chem. 274:26968.
GenBank Accession # P35052.
David, G. et al. (1990) J. Cell Biol. 111:3165.
Lories, V. et al. (1992) J. Biol. Chem. 267:1116.
Lories, V. et al. (1989) J. Biol. Chem. 264:7009.
GenBank Accession # EAW71184.
GenBank Accession # EAW71183.
Chernousov, M.A. et al. (2006) J. Neurosci. 26:508.
Wegrowski, Y. et al. (2006) Clin. Exp. Immunol. 144:485.
Qiao, D. et al. (2003) J. Biol. Chem. 278:16045.
Kayed, H. et al. (2006) Int. J. Oncol. 29:1139.
Selleck, S.B. (2006) SciSTKE, April 4:pe17.
Qiao, D. et al. (2003) J. Biol. Chem. 278:16045.
Su, G. et al. (2006) Am. J. Pathol. 168:2014.
Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
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